TY - JOUR
T1 - The Study of Protein Conformation in Solution Via Direct Sampling by Desorption Electrospray Ionization Mass Spectrometry
AU - Miao, Zhixin
AU - Wu, Shiyong
AU - Chen, Hao
N1 - Funding Information:
The authors acknowledge support for this work by NSF ( CHE-0911160 ). The authors gratefully acknowledge Professor Michael L. Gross at Washington University in St. Louis for the access to the NIH/NCRR Mass Spectrometry Resources (grant number 2P41RR000954 ) and are also thankful to Mr. Hao Zhang for his kind help.
PY - 2010/10
Y1 - 2010/10
N2 - The direct sampling feature of liquid sample desorption electrospray ionization (DESI) allows the ionization of liquid samples without adding acids/organic solvents (i.e., without sample pretreatment). As a result, it provides a new approach for probing protein conformation in solution. In this study, it has been observed that native protein ions are generated from proteins in water by DESI. Interestingly, the intensities of the resulting protein ions appear to be higher than those generated by ESI of the proteins in water or in ammonium acetate. For protein solutions that already contain acids/organic solvents, DESI can be used to investigate the influences of these denaturants on protein conformations and the obtained results are in good agreement with spectroscopic data. In addition, online monitoring of protein conformational changes by DESI is feasible; for instance, heat-induced unfolding of ubiquitin can be traced with DESI in water without influences of organic solvents/acids. This DESI method provides a new alternative tool for the study of protein conformation in solution.
AB - The direct sampling feature of liquid sample desorption electrospray ionization (DESI) allows the ionization of liquid samples without adding acids/organic solvents (i.e., without sample pretreatment). As a result, it provides a new approach for probing protein conformation in solution. In this study, it has been observed that native protein ions are generated from proteins in water by DESI. Interestingly, the intensities of the resulting protein ions appear to be higher than those generated by ESI of the proteins in water or in ammonium acetate. For protein solutions that already contain acids/organic solvents, DESI can be used to investigate the influences of these denaturants on protein conformations and the obtained results are in good agreement with spectroscopic data. In addition, online monitoring of protein conformational changes by DESI is feasible; for instance, heat-induced unfolding of ubiquitin can be traced with DESI in water without influences of organic solvents/acids. This DESI method provides a new alternative tool for the study of protein conformation in solution.
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U2 - 10.1016/j.jasms.2010.06.003
DO - 10.1016/j.jasms.2010.06.003
M3 - Article
C2 - 20620076
AN - SCOPUS:77956875402
SN - 1044-0305
VL - 21
SP - 1730
EP - 1736
JO - Journal of the American Society for Mass Spectrometry
JF - Journal of the American Society for Mass Spectrometry
IS - 10
ER -